Tag | Content |
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CPLM ID | CPLM-001817 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoenolpyruvate carboxylase |
Protein Synonyms/Alias | PEPC; PEPCase |
Gene Name | ppc |
Gene Synonyms/Alias | glu; b3956; JW3928 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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17 | SNVSMLGKVLGETIK | acetylation | [1, 2] | 24 | KVLGETIKDALGEHI | acetylation | [1, 2] | 94 | QYHSISPKGEAASNP | acetylation | [2] | 112 | ARTLRKLKNQPELSE | acetylation | [2] | 123 | ELSEDTIKKAVESLS | acetylation | [2] | 164 | CLKQLDNKDIADYEH | acetylation | [2] | 193 | WHTDEIRKLRPSPVD | acetylation | [1] | 203 | PSPVDEAKWGFAVVE | acetylation | [2] | 235 | LEENLGYKLPVEFVP | acetylation | [2] | 274 | VLLLSRWKATDLFLK | acetylation | [2] | 317 | EPYRYLMKNLRSRLM | acetylation | [1, 2] | 384 | LDTLRRVKCFGVPLV | acetylation | [2] | 437 | LIRELNSKRPLLPRN | acetylation | [2] | 570 | ALIKTCEKAGIELTL | acetylation | [2] | 605 | SQPPGSLKGGLRVTE | acetylation | [2] | 676 | RGYVRENKDFVPYFR | acetylation | [2] | 693 | TPEQELGKLPLGSRP | acetylation | [2] | 740 | GAGTALQKVVEDGKQ | acetylation | [2] | 746 | QKVVEDGKQSELEAM | acetylation | [2] | 789 | YDQRLVDKALWPLGK | acetylation | [1, 2] | 796 | KALWPLGKELRNLQE | acetylation | [2] | 855 | HRSRQAEKEGQEPDP | acetylation | [2] |
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Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. |
Sequence Annotation | ACT_SITE 138 138 ACT_SITE 546 546 By similarity. |
Keyword | 3D-structure; Allosteric enzyme; Carbon dioxide fixation; Complete proteome; Lyase; Magnesium; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 883 AA |
Protein Sequence | MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND ANRQELLTTL 60 QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPELSED 120 TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ 180 LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF 240 VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL 300 ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE ELWEPLYACY 360 QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES 420 WSEADKQAFL IRELNSKRPL LPRNWQPSAE TREVLDTCQV IAEAPQGSIA AYVISMAKTP 480 SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG 540 YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP 600 PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK ESWRRIMDEL 660 SVISCDVYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA 720 WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE 780 YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN 840 VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG 883 |
Gene Ontology | GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:HAMAP. GO:0015977; P:carbon fixation; IEA:HAMAP. GO:0006107; P:oxaloacetate metabolic process; IEA:HAMAP. GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |